(ADP-ribosyl)hydrolases: structure, function, and biology.
ADP-ribose
ADP-ribosylation
ARH3
DNA damage
DraG
PARG
PARP
catalytic mechanism
genome stability
macrodomain
structural biology
Journal
Genes & development
ISSN: 1549-5477
Titre abrégé: Genes Dev
Pays: United States
ID NLM: 8711660
Informations de publication
Date de publication:
01 03 2020
01 03 2020
Historique:
pubmed:
8
2
2020
medline:
24
4
2020
entrez:
8
2
2020
Statut:
ppublish
Résumé
ADP-ribosylation is an intricate and versatile posttranslational modification involved in the regulation of a vast variety of cellular processes in all kingdoms of life. Its complexity derives from the varied range of different chemical linkages, including to several amino acid side chains as well as nucleic acids termini and bases, it can adopt. In this review, we provide an overview of the different families of (ADP-ribosyl)hydrolases. We discuss their molecular functions, physiological roles, and influence on human health and disease. Together, the accumulated data support the increasingly compelling view that (ADP-ribosyl)hydrolases are a vital element within ADP-ribosyl signaling pathways and they hold the potential for novel therapeutic approaches as well as a deeper understanding of ADP-ribosylation as a whole.
Identifiants
pubmed: 32029451
pii: gad.334631.119
doi: 10.1101/gad.334631.119
pmc: PMC7050489
doi:
Substances chimiques
Adenosine Diphosphate
61D2G4IYVH
Hydrolases
EC 3.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
263-284Subventions
Organisme : Wellcome Trust
ID : 210634
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R007195/1
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 101794
Pays : United Kingdom
Organisme : Cancer Research UK
ID : C35050/A22284
Pays : United Kingdom
Informations de copyright
© 2020 Rack et al.; Published by Cold Spring Harbor Laboratory Press.
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